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- PDB-3cjt: Ribosomal protein L11 methyltransferase (PrmA) in complex with di... -

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Basic information

Entry
Database: PDB / ID: 3cjt
TitleRibosomal protein L11 methyltransferase (PrmA) in complex with dimethylated ribosomal protein L11
Components
  • 50S ribosomal protein L11
  • Ribosomal protein L11 methyltransferase
KeywordsTRANSFERASE/RIBOSOMAL PROTEIN / S-Adenosyl-L-Methionine dependent methyltransferase / post-translational modification / multi-specific trimethylation / Ribonucleoprotein / Ribosomal protein / RNA-binding / rRNA-binding / TRANSFERASE-RIBOSOMAL PROTEIN COMPLEX
Function / homology
Function and homology information


protein-lysine N-methyltransferase activity / Transferases; Transferring one-carbon groups; Methyltransferases / large ribosomal subunit rRNA binding / methylation / cytosolic large ribosomal subunit / structural constituent of ribosome / translation / cytoplasm
Similarity search - Function
Ribosomal protein L11 methyltransferase / : / Sun protein; domain 3 / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12, N-terminal domain / Ribosomal protein L11/L12, C-terminal domain / Ribosomal protein L11 methyltransferase (PrmA) / Ribosomal protein L11, bacterial-type / Ribosomal protein L11, conserved site / Ribosomal protein L11 signature. ...Ribosomal protein L11 methyltransferase / : / Sun protein; domain 3 / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12, N-terminal domain / Ribosomal protein L11/L12, C-terminal domain / Ribosomal protein L11 methyltransferase (PrmA) / Ribosomal protein L11, bacterial-type / Ribosomal protein L11, conserved site / Ribosomal protein L11 signature. / Vaccinia Virus protein VP39 / Ribosomal protein L11, N-terminal / Ribosomal protein L11, N-terminal domain / Ribosomal protein L11/L12 / Ribosomal protein L11, C-terminal / Ribosomal protein L11, C-terminal domain superfamily / Ribosomal protein L11/L12, N-terminal domain superfamily / Ribosomal protein L11/L12 / Ribosomal protein L11, RNA binding domain / Arc Repressor Mutant, subunit A / Alpha-Beta Plaits / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
N,N-dimethyl-L-methionine / NITRATE ION / S-ADENOSYL-L-HOMOCYSTEINE / S-ADENOSYLMETHIONINE / Large ribosomal subunit protein uL11 / Ribosomal protein L11 methyltransferase
Similarity search - Component
Biological speciesThermus thermophilus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsDemirci, H. / Gregory, S.T. / Dahlberg, A.E. / Jogl, G.
CitationJournal: Structure / Year: 2008
Title: Multiple-Site Trimethylation of Ribosomal Protein L11 by the PrmA Methyltransferase.
Authors: Demirci, H. / Gregory, S.T. / Dahlberg, A.E. / Jogl, G.
History
DepositionMar 13, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 20, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Aug 30, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ribosomal protein L11 methyltransferase
B: 50S ribosomal protein L11
C: Ribosomal protein L11 methyltransferase
D: 50S ribosomal protein L11
E: Ribosomal protein L11 methyltransferase
F: 50S ribosomal protein L11
G: Ribosomal protein L11 methyltransferase
H: 50S ribosomal protein L11
I: Ribosomal protein L11 methyltransferase
J: 50S ribosomal protein L11
K: Ribosomal protein L11 methyltransferase
L: 50S ribosomal protein L11
M: Ribosomal protein L11 methyltransferase
N: 50S ribosomal protein L11
O: Ribosomal protein L11 methyltransferase
P: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)349,56942
Polymers344,96716
Non-polymers4,60226
Water33,9581885
1
A: Ribosomal protein L11 methyltransferase
B: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)44,00210
Polymers43,1212
Non-polymers8818
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4510 Å2
ΔGint-25.3 kcal/mol
Surface area18220 Å2
MethodPISA
2
C: Ribosomal protein L11 methyltransferase
D: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,5193
Polymers43,1212
Non-polymers3981
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1780 Å2
ΔGint-14.4 kcal/mol
Surface area15710 Å2
MethodPISA
3
E: Ribosomal protein L11 methyltransferase
F: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8076
Polymers43,1212
Non-polymers6864
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4150 Å2
ΔGint-28.9 kcal/mol
Surface area18190 Å2
MethodPISA
4
G: Ribosomal protein L11 methyltransferase
H: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,5193
Polymers43,1212
Non-polymers3981
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1760 Å2
ΔGint-13.1 kcal/mol
Surface area15810 Å2
MethodPISA
5
I: Ribosomal protein L11 methyltransferase
J: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8778
Polymers43,1212
Non-polymers7576
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4110 Å2
ΔGint-28.2 kcal/mol
Surface area18120 Å2
MethodPISA
6
K: Ribosomal protein L11 methyltransferase
L: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,5193
Polymers43,1212
Non-polymers3981
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1820 Å2
ΔGint-15.2 kcal/mol
Surface area15630 Å2
MethodPISA
7
M: Ribosomal protein L11 methyltransferase
N: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8076
Polymers43,1212
Non-polymers6864
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3950 Å2
ΔGint-27.6 kcal/mol
Surface area18430 Å2
MethodPISA
8
O: Ribosomal protein L11 methyltransferase
P: 50S ribosomal protein L11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,5193
Polymers43,1212
Non-polymers3981
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1810 Å2
ΔGint-14.6 kcal/mol
Surface area15470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.822, 69.943, 379.007
Angle α, β, γ (deg.)90.00, 90.47, 90.00
Int Tables number3
Space group name H-MP121

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Components

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Protein , 2 types, 16 molecules ACEGIKMOBDFHJLNP

#1: Protein
Ribosomal protein L11 methyltransferase / L11 Mtase


Mass: 27594.738 Da / Num. of mol.: 8 / Mutation: H104A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Gene: prmA / Plasmid: pET30b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) Star
References: UniProt: Q84BQ9, Transferases; Transferring one-carbon groups; Methyltransferases
#2: Protein
50S ribosomal protein L11


Mass: 15526.111 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Gene: rplK, rpl11 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) prmA::TC / References: UniProt: P36238

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Non-polymers , 7 types, 1911 molecules

#3: Chemical
ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: NO3
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#5: Chemical
ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE


Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H20N6O5S
#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical
ChemComp-2MM / N,N-dimethyl-L-methionine


Mass: 177.264 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C7H15NO2S
#8: Chemical
ChemComp-SAM / S-ADENOSYLMETHIONINE


Mass: 398.437 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C15H22N6O5S
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1885 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.68 Å3/Da / Density % sol: 54.15 %
Crystal growTemperature: 277 K / Method: microbatch under oil / pH: 5.8
Details: 200mM magnesium nitrate hexahydrate, 20% w/v PEG3350, 4mM AdoMet, pH 5.8, microbatch under oil, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9797 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 15, 2007
Details: Rosenbaum-Rock double crystal sagittal focusing monochrometer and vertical focusing mirror
RadiationMonochromator: Rosenbaum-Rock double crystal sagittal focusing monochrometer and vertical focusing mirror
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9797 Å / Relative weight: 1
ReflectionResolution: 2.3→30 Å / Num. obs: 157914 / % possible obs: 96.5 % / Observed criterion σ(I): -3 / Redundancy: 6.7 % / Rmerge(I) obs: 0.071 / Net I/σ(I): 25
Reflection shellResolution: 2.3→2.38 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.364 / Mean I/σ(I) obs: 2.7 / Num. unique all: 12404 / % possible all: 76.7

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
ADSCQuantumdata collection
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entries 2NXC, 2NXN

2nxc

2nxn


Resolution: 2.3→29.74 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.905 / SU B: 11.637 / SU ML: 0.162 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.3 / ESU R Free: 0.243 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2593 7909 5 %RANDOM
Rwork0.19442 ---
obs0.19765 149975 96.31 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.08 Å2
Baniso -1Baniso -2Baniso -3
1-0.01 Å20 Å2-0.01 Å2
2--0 Å20 Å2
3----0.01 Å2
Refinement stepCycle: LAST / Resolution: 2.3→29.74 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21338 0 296 1885 23519
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.02222163
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5381.99630175
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.32652795
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.51422.861846
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.687153386
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.19515172
X-RAY DIFFRACTIONr_chiral_restr0.0950.23336
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0216884
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2140.210339
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3010.214556
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2430.21716
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2470.2258
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2110.266
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6471.514469
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.071222368
X-RAY DIFFRACTIONr_scbond_it1.71538948
X-RAY DIFFRACTIONr_scangle_it2.8024.57806
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.3→2.355 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.337 449 -
Rwork0.241 8149 -
obs-8149 71.84 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.97830.8250.20551.6675-1.02675.02880.0527-0.08280.029-0.10450.01020.0438-0.1683-0.188-0.0628-0.05910.0323-0.00960.0011-0.0034-0.092-15.51563.0162-1.8632
20.80220.0989-0.1070.7943-0.07020.72210.0423-0.01070.00220.0881-0.0689-0.0711-0.0302-0.02960.0265-0.0579-0.0226-0.0225-0.02570.0167-0.0114-9.8064-1.50541.6133
30.5253-0.2482-0.34111.86240.36733.2770.08230.0789-0.0335-0.0948-0.0188-0.04910.05930.0022-0.0635-0.08-0.0134-0.00420.01460.0212-0.0369-9.6725-3.131913.9721
44.20580.8959-1.12782.8607-0.58778.01350.6895-0.28980.01670.33640.00940.170.9406-0.2993-0.69890.0746-0.0273-0.2393-0.15030.0176-0.0749-18.8028-17.1195-7.8898
53.82041.1076-0.50125.34371.36196.74740.0386-0.31670.3665-0.341-0.1088-0.3322-0.4804-0.05080.0702-0.2079-0.03530.0337-0.090.0093-0.004343.796215.57658.7521
60.6346-0.4068-0.00991.1012-0.65361.23240.0615-0.01920.00970.05260.02170.0626-0.04160.0066-0.0831-0.0081-0.0552-0.0133-0.08870.0092-0.02735.211413.454565.2445
74.35021.47620.25537.3314-2.08453.83980.2418-0.70960.57220.489-0.3198-0.2509-0.4586-0.17610.0781-0.1397-0.0977-0.00550.077-0.1747-0.128334.76217.145974.1783
82.31040.36540.80751.8652-0.23185.2864-0.0215-0.0284-0.03270.01120.0991-0.06730.16630.1278-0.07760.0040.02860.0024-0.05320.0137-0.119916.6665-30.088996.6312
91.0954-0.01790.00640.63470.10510.5755-0.05650.09660.0773-0.00320.01340.01010.04230.01590.0431-0.0286-0.0283-0.0181-0.05680.0278-0.011712.6522-24.058253.2423
101.6439-0.3446-0.15181.0207-0.25242.918-0.0059-0.112-0.01450.09390.05210.0358-0.0355-0.068-0.0462-0.0009-0.0312-0.0247-0.05720.0051-0.049410.7703-24.105180.811
112.27071.4751.05074.05412.48139.54570.02990.3787-0.0173-0.08950.58420.14150.1432-1.3306-0.6141-0.1538-0.1011-0.03430.140.2962-0.104-4.1489-34102.2058
125.69320.5547-2.65324.28611.34457.63740.0336-0.22140.2609-0.06340.0128-0.31630.00960.4228-0.0463-0.0934-0.0439-0.0425-0.2399-0.0079-0.00929.817529.694536.2238
131.1108-0.40710.55520.66380.00431.12930.00710.0633-0.105-0.03020.06360.0201-0.01060.0426-0.0707-0.09-0.0465-0.00980.0020.011-0.029527.6714-8.919429.6283
145.85481.11991.64263.21850.3094.1411-0.3220.3080.2163-0.63590.3029-0.37080.16540.4150.01910.0619-0.09650.1154-0.1816-0.0046-0.085731.523320.669820.7581
152.6298-0.2172-1.05352.4637-0.35395.1265-0.03720.05960.05720.05880.1311-0.0975-0.1080.1184-0.09380.0005-0.0249-0.0029-0.05990.0121-0.119116.82851.037693.1227
161.2025-0.0138-0.02440.86030.07180.7563-0.0625-0.0868-0.09750.03340.01680.0324-0.04580.0290.0457-0.01530.02670.0266-0.06380.0378-0.036111.7573-4.952136.4565
171.53440.0930.32961.40320.39713.51870.00650.10070.0002-0.06980.05920.05580.0319-0.0716-0.0657-0.01570.01510.0251-0.06260.015-0.055710.4621-4.8584108.8865
182.4561-0.7372-1.59954.01992.668211.706-0.051-0.2891-0.07320.22150.5361-0.0665-0.3382-1.3008-0.485-0.14890.06230.0020.13140.2344-0.1556-3.22714.478786.8185
195.3943-2.28032.62694.48061.08017.13150.00610.1484-0.42510.095-0.1373-0.3748-0.07720.49470.1313-0.04660.0377-0.0019-0.32630.04080.029828.7717-58.7589153.6067
201.420.5379-0.73380.79470.08031.35840.0141-0.08640.10160.01440.06720.00450.01410.076-0.0814-0.07910.05250.02180.00290.0213-0.060726.6115-20.1315160.0707
218.56-1.5186-3.84976.45421.60686.0783-0.3954-0.7632-0.29690.65620.3059-0.381-0.27250.81450.08960.07640.1149-0.2243-0.19550.0301-0.214630.434-49.6802168.997
223.1763-0.8271-0.01023.0779-0.49255.63420.1170.0555-0.09670.0774-0.0780.09740.1372-0.1829-0.039-0.0468-0.03450.0274-0.0041-0.0037-0.1565-17.1776-32.0354191.2249
230.82210.02630.05111.0534-0.06520.79360.01550.00770.0298-0.0971-0.0608-0.07630.0399-0.03390.0453-0.03860.02380.049-0.04020.0262-0.0343-10.8261-27.4844147.9184
240.47780.11570.18931.94420.01023.33050.0126-0.06880.03450.10550.00220.02-0.06730.0502-0.0148-0.04360.02620.01910.00510.0166-0.0711-11.0616-25.9135175.4395
255.7034-1.84582.82522.7525-1.746811.88760.55750.23750.2881-0.398-0.0134-0.0977-1.311-0.2929-0.54410.15970.05640.2596-0.2020.0051-0.1522-20.9566-11.1252196.8791
262.6675-0.80390.8576.17892.6978.05360.00270.2549-0.44160.4413-0.1734-0.36380.40420.08390.1708-0.24720.02510.0055-0.09470.02440.001442.9793-44.6042130.932
270.69230.4716-0.03291.3859-0.76771.42080.06710.00730.0118-0.10.02230.12180.05420.0246-0.08940.00950.04840.0298-0.10510.0191-0.04474.4261-42.4558124.3235
284.1595-3.16110.40498.1697-3.72065.2430.27020.8678-0.7662-0.4445-0.2077-0.25290.7081-0.2079-0.0625-0.12480.04570.01340.08-0.256-0.187733.9956-46.2693115.4792
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 541 - 54
2X-RAY DIFFRACTION2AA67 - 25467 - 254
3X-RAY DIFFRACTION3BB2 - 702 - 70
4X-RAY DIFFRACTION4BB72 - 14072 - 140
5X-RAY DIFFRACTION5CC1 - 541 - 54
6X-RAY DIFFRACTION6CC67 - 25467 - 254
7X-RAY DIFFRACTION7DD2 - 702 - 70
8X-RAY DIFFRACTION8EE1 - 541 - 54
9X-RAY DIFFRACTION9EE67 - 25467 - 254
10X-RAY DIFFRACTION10FF2 - 702 - 70
11X-RAY DIFFRACTION11FF72 - 14072 - 140
12X-RAY DIFFRACTION12GG1 - 541 - 54
13X-RAY DIFFRACTION13GG67 - 25467 - 254
14X-RAY DIFFRACTION14HH2 - 702 - 70
15X-RAY DIFFRACTION15II1 - 541 - 54
16X-RAY DIFFRACTION16II67 - 25467 - 254
17X-RAY DIFFRACTION17JJ2 - 702 - 70
18X-RAY DIFFRACTION18JJ72 - 14072 - 140
19X-RAY DIFFRACTION19KK1 - 541 - 54
20X-RAY DIFFRACTION20KK67 - 25467 - 254
21X-RAY DIFFRACTION21LL2 - 702 - 70
22X-RAY DIFFRACTION22MM1 - 541 - 54
23X-RAY DIFFRACTION23MM67 - 25467 - 254
24X-RAY DIFFRACTION24NN2 - 702 - 70
25X-RAY DIFFRACTION25NN72 - 14072 - 140
26X-RAY DIFFRACTION26OO1 - 541 - 54
27X-RAY DIFFRACTION27OO67 - 25467 - 254
28X-RAY DIFFRACTION28PP2 - 702 - 70

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